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Conformationally restrained peptides: crystal structure of tert-butyloxycarbonyl-L-alanyl-D-alanyl-D-aminosuccinyl-glycyl-L- alanine methyl ester. 1996

D Demasi, and S Capasso, and F Sica, and A Zagari
Centre for the Study of Biocrystallography, CNR, Naples, Italy.

The solid-state structure of a heterochiral peptide embodying a D-aminosuccinyl peptide (D-Asu) and a D-Ala was studied in order to analyse the effects of Asu and amino acids with inverse chirality on peptide conformation. The crystal structure has been determined by X-ray diffraction techniques and refined to a final R factor of 0.043. The molecule adopts an unusual overall "S-shape' conformation due to two consecutive type II beta-turns. In this molecule it is possible to compare a type II beta-bend conformation (L-Ala1-D-Ala2) favoured by the presence of a D-residue at second corner to a type II beta-turn (D-Asu3-Gly4) favoured by the presence of a D-Asu residue at first corner. In agreement with previous studies, this structure confirms that the Asu has a high propensity to adopt a type II or II' beta-bend conformation and that it may be used as a strong determinant of these structural motifs.

UI MeSH Term Description Entries
D009842 Oligopeptides Peptides composed of between two and twelve amino acids. Oligopeptide
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations

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